Your Input: | |||||
amtB | Ammonium transporter; Involved in the uptake of ammonia; Belongs to the ammonia transporter channel (TC 1.A.11.2) family. (428 aa) | ||||
lptD | LPS assembly OM complex LptDE, beta-barrel component; Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Contributes to n-hexane resistance. (784 aa) | ||||
fhuA | Ferrichrome outer membrane transporter; Involved in the uptake of iron in complex with ferrichrome, a hydroxamate-type siderophore. Binds and transports ferrichrome-iron across the outer membrane. In addition to its role in ferrichrome-iron transport, transports the antibiotic albomycin, which is a structural analog of ferrichrome, and acts as a receptor for colicin M, microcin J25 and bacteriophages T1, T5, phi80 and UC-1. The energy source, which is required for all FhuA functions except infection by phage T5, is provided by the inner membrane TonB system. (747 aa) | ||||
btuF | Vitamin B12 ABC transporter periplasmic binding protein; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Binds vitamin B12 and delivers it to the periplasmic surface of BtuC. (266 aa) | ||||
lacY | Lactose permease; Responsible for transport of beta-galactosides into the cell, with the concomitant import of a proton (symport system). Can transport lactose, melibiose, lactulose or the analog methyl-1-thio-beta,D- galactopyranoside (TMG), but not sucrose or fructose. The substrate specificity is directed toward the galactopyranosyl moiety of the substrate. (417 aa) | ||||
acrA | Multidrug efflux system; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm. (397 aa) | ||||
lptE | LPS assembly OM complex LptDE, lipoprotein component; Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane. Belongs to the LptE lipoprotein family. (193 aa) | ||||
tolR | Membrane spanning protein in TolA-TolQ-TolR complex; Part of the Tol-Pal system, which plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity. Required, with TolQ, for the proton motive force-dependent activation of TolA and for TolA-Pal interaction .The Tol-Pal system is also required for polar localization of chemoreceptors clusters (Probable). There are about 900 TolR molecules per cell. Modeling suggests that non-covalent binding of OmpA (from the outer membrane) and TolR (from the inner membrane) to peptidoglycan [...] (142 aa) | ||||
acrZ | AcrAB-TolC efflux pump accessory protein, membrane-associated; AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with a broad substrate specificity. This protein binds to AcrB and is required for efflux of some but not all substrates, suggesting it may influence the specificity of drug export. (49 aa) | ||||
ompX | Outer membrane protein X; Belongs to the outer membrane OOP (TC 1.B.6) superfamily. OmpX family. (171 aa) | ||||
aqpZ | Aquaporin Z; Channel that permits osmotically driven movement of water in both directions. It is involved in the osmoregulation and in the maintenance of cell turgor during volume expansion in rapidly growing cells. It mediates rapid entry or exit of water in response to abrupt changes in osmolarity. (231 aa) | ||||
lolA | Lipoprotein chaperone; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane); the inner membrane retention signal functions at the release step. (203 aa) | ||||
ompF | Outer membrane porin 1a (Ia;b;F); Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (362 aa) | ||||
ompA | Outer membrane protein A (3a;II*;G;d); With TolR probably plays a role in maintaining the position of the peptidoglycan cell wall in the periplasm (Probable). Plays a role in resistance to environmental stress, and a role in outer membrane functionality and cell shape. Non-covalently binds peptidoglycan (Probable). Acts as a porin with low permeability that allows slow penetration of small solutes. A very abundant protein, there can be up to 210,000 OmpA molecules per cell. Reconstitution in unilamellar lipid vesicles shows only about 3% of the protein is in an open conformation, whic [...] (346 aa) | ||||
murJ | Putative lipid II flippase; Involved in peptidoglycan biosynthesis. Transports lipid- linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane. Belongs to the MurJ/MviN family. (511 aa) | ||||
lolB | Lipoprotein localization factor; Plays a critical role in the incorporation of lipoproteins in the outer membrane after they are released by the LolA protein. Essential for E.coli viability; Belongs to the LolB family. (207 aa) | ||||
mdtK | Multidrug efflux system transporter; Multidrug efflux pump that probably functions as a Na(+)/drug antiporter. Confers resistance to many drugs such as fluoroquinolones (norfloxacin, ciprofloxacin, enoxacin) and tetraphenylphosphonium ion (TPP). Also to deoxycholate, doxorubicin, trimethoprim, chloramphenicol, fosfomycin, ethidium bromide and benzalkonium. Also able to export peptides; when overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth. Cells overexpressing [...] (457 aa) | ||||
btuC | Vitamin B12 ABC transporter permease; Part of the ABC transporter complex BtuCDF involved in vitamin B12 import. Involved in the translocation of the substrate across the membrane; Belongs to the binding-protein-dependent transport system permease family. FecCD subfamily. (326 aa) | ||||
ompC | Outer membrane porin protein C; Forms pores that allow passive diffusion of small molecules across the outer membrane. (Microbial infection) A mixed OmpC-OmpF heterotrimer is the outer membrane receptor for toxin CdiA-EC536; polymorphisms in extracellular loops 4 and 5 of OmpC confer susceptibility to CdiA- EC536-mediated toxicity; Belongs to the Gram-negative porin family. (367 aa) | ||||
mlaA | ABC transporter maintaining OM lipid asymmetry, OM lipoprotein component; Involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Belongs to the MlaA family. (251 aa) | ||||
uraA | Uracil permease; Transport of uracil in the cell. Belongs to the xanthine/uracil permease family. Nucleobase:cation symporter-2 (NCS2) (TC 2.A.40) subfamily. (429 aa) | ||||
tolC | Transport channel; Outer membrane channel, which is required for the function of several efflux systems such as AcrAB-TolC, AcrEF-TolC, EmrAB-TolC and MacAB-TolC. These systems are involved in export of antibiotics and other toxic compounds from the cell. TolC is also involved in import of colicin E1 into the cells. (493 aa) | ||||
mlaC | ABC transporter maintaining OM lipid asymmetry, periplasmic binding protein; Involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. May transfer phospholipid across the periplasmic space and deliver it to the MlaFEDB complex at the inner membrane. Belongs to the MlaC/ttg2D family. (211 aa) | ||||
mlaD | OM lipid asymmetry maintenance protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. MlaD functions in substrate binding with strong affinity for phospholipids and modulates ATP hydrolytic activity of the complex. (183 aa) | ||||
mlaE | ABC transporter maintaining OM lipid asymmetry, inner membrane permease protein; Part of the ABC transporter complex MlaFEDB, which is involved in a phospholipid transport pathway that maintains lipid asymmetry in the outer membrane by retrograde trafficking of phospholipids from the outer membrane to the inner membrane. Probably responsible for the translocation of the substrate across the membrane. Belongs to the MlaE permease family. (260 aa) | ||||
lptA | Lipopolysaccharide export ABC transporter periplasmic binding protein; Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm. (185 aa) | ||||
secY | Preprotein translocase membrane subunit; The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently. SecY is r [...] (443 aa) | ||||
tatA | TatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system. Belongs to the TatA/E family. (89 aa) | ||||
tatB | TatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatC, TatB is part of a receptor directly interacting with Tat signal peptides. TatB may form an oligomeric binding site that transiently accommodates folded Tat precursor proteins before their translocation. (171 aa) | ||||
tatC | TatABCE protein translocation system subunit; Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin- arginine motif in their signal peptide across membranes. Together with TatB, TatC is part of a receptor directly interacting with Tat signal peptides. (258 aa) | ||||
btuB | Vitamin B12/cobalamin outer membrane transporter; Involved in the active translocation of vitamin B12 (cyanocobalamin) across the outer membrane to the periplasmic space. It derives its energy for transport by interacting with the trans- periplasmic membrane protein TonB. Is also a receptor for bacteriophages BF23 and C1, and for A and E colicins. (614 aa) | ||||
malE | Maltose transporter subunit; Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Binds maltose and higher maltodextrins such as maltotriose. Belongs to the bacterial solute-binding protein 1 family. (396 aa) | ||||
fecA | TonB-dependent outer membrane ferric citrate transporter and signal transducer; FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system. (774 aa) |